Human liver aldehyde dehydrogenase: partial purification and properties

1969 ◽  
Vol 47 (3) ◽  
pp. 265-272 ◽  
Author(s):  
A. H. Blair ◽  
F. H. Bodley
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Human Liver ◽  
Deae Cellulose ◽  
Maximal Activity ◽  
Partial Purification ◽  
Aliphatic Aldehydes ◽  
Low Concentrations ◽  
Purification And Properties ◽  
Liver Aldehyde Dehydrogenase ◽  
Metabolic Reduction

Aldehyde dehydrogenase was partially purified from human liver. During purification, activity was resolved into one major and one minor species by DEAE-cellulose column chromatography; the properties of the predominant form were investigated.Aldehydes are oxidized when NAD+, but not NADP+, is the electron acceptor, maximal activity occurring between pH 9 and 10. Several aliphatic aldehydes and hydroxyaldehydes served as substrates for the enzyme. Benzaldehyde also was oxidized, but at a comparatively low rate. Aliphatic aldehydes carrying negatively charged groups are not oxidized. The enzyme is sensitive to low concentrations of two sulfhydryl reagents, p-chloromercuribenzoate and mercuric ions; this inhibition was reversed with sulfhydryl compounds. Like other aldehyde dehydrogenases, the human liver enzyme is inhibited by arsenite and the inhibition is potentiated by mercaptoethanol. Only 35% inhibition was produced by disulfiram at 40 μM; and diethyldithiocarbamate, its metabolic reduction product, had no effect on activity below 10 mM.

scholarly journals The activation of aldehyde dehydrogenase by diethylstilboestrol and 2,2′-dithiodipyridine

1982 ◽  
Vol 207 (1) ◽  
pp. 81-89 ◽  
Author(s):  
T M Kitson
Keyword(s):  
Enzyme Activity ◽  
Aldehyde Dehydrogenase ◽  
Human Liver ◽  
Common Property ◽  
Rabbit Liver ◽  
Aldehyde Dehydrogenases ◽  
Cytoplasmic Enzyme ◽  
Sheep Liver ◽  
Low Concentrations ◽  
Liver Aldehyde Dehydrogenase

1. The activation of sheep liver cytoplasmic aldehyde dehydrogenase by diethylstilboestrol and by 2,2′-dithiodipyridine is described. The effects of the two modifiers are very similar with respect to variation with acetaldehyde concentration, pH and temperature. Thus the degree of activation is maximal when the enzyme is assayed at approx. 1 mM-acetaldehyde, is greater at 25 degrees C than at 37 degrees C, and is greater at pH 7.4 than at pH 9.75. With low concentrations of acetaldehyde both modifiers decrease the enzyme activity. 2. Diethylstilboestrol affects the sheep liver cytoplasmic enzyme in a very similar way to that previously described for a rabbit liver cytoplasmic enzyme. Preliminary experiments show that the same is true for a preparation of human liver aldehyde dehydrogenase. It is proposed that sensitivity to diethylstilboestrol (and steroids) is a common property of all mammalian cytoplasmic aldehyde dehydrogenases.

Spatial distribution of human liver aldehyde dehydrogenase isoenzymes

1999 ◽  
Vol 111 (6) ◽  
pp. 461-466 ◽  
Author(s):  
I. Piotr Maly ◽  
Valérie Crotet ◽  
D. Sasse
Keyword(s):  
Spatial Distribution ◽  
Aldehyde Dehydrogenase ◽  
Human Liver ◽  
Liver Aldehyde Dehydrogenase

Tryptophan synthase: partial purification and some properties of the B-protein subunit from pea plants (Pisum sativum cv. Alaska)

1972 ◽  
Vol 50 (3) ◽  
pp. 587-594 ◽  
Author(s):  
James Chen ◽  
W. G. Boll
Keyword(s):  
Pyridoxal Phosphate ◽  
Sulfate Solution ◽  
Maximal Activity ◽  
Partial Purification ◽  
Tryptophan Synthase ◽  
Ammonium Sulfate Solution ◽  
Protein Subunit ◽  
Protein Activity ◽  
Low Concentrations ◽  
Sulfhydryl Compounds

A method was developed for partial purification of the B-protein of tryptophan synthase (EC 4.2.1.20) from pea plants. The enzyme was purified 28-fold with about 21% recovery. The purification procedure removed both A-protein activity, and denatured A-protein, from the B-protein. The B-protein is unstable and activity was not preserved by either dithiothreitol, mercaptoethanol, or L-cysteine. These sulfhydryl compounds were inhibitory at relatively low concentrations. Both pyridoxal phosphate and glycerol preserved the activity to some extent. Glycerol itself was inhibitory. However, when enzyme was stored with 25% glycerol in the cold the activity actually increased within the first 24 h. The enzyme is most stable as a suspension in ammonium sulfate solution. The partially purified B-protein, in the absence of A-protein, catalyzed the condensation of indole and serine to tryptophan at an appreciable rate. Pyridoxal phosphate was required for maximal activity while both pyridoxine phosphate and pyridoxamine phosphate were inactive in the system. The molecular weight of the B-protein was estimated to be about 101 000, which is close to that of the B-protein subunit of Escherichia coli. Differences in properties between bacterial, tobacco, and pea TSase are discussed.

Human liver aldehyde dehydrogenase: Subcellular distribution in alcoholics and nonalcoholics

Alcohol ◽  
1988 ◽  
Vol 5 (1) ◽  
pp. 73-80 ◽  
Author(s):  
D. Meier-Tackmann ◽  
G.C. Korenke ◽  
D.P. Agarwal ◽  
H. Werner Goedde
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Subcellular Distribution ◽  
Human Liver ◽  
Liver Aldehyde Dehydrogenase

scholarly journals Purification and characterization of a rat brain aldehyde dehydrogenase able to metabolize γ-aminobutyraldehyde to γ-aminobutyric acid

1990 ◽  
Vol 269 (1) ◽  
pp. 25-29 ◽  
Author(s):  
T Abe ◽  
K Takada ◽  
K Ohkawa ◽  
M Matsuda
Keyword(s):  
Substrate Specificity ◽  
Rat Brain ◽  
Aldehyde Dehydrogenase ◽  
Human Liver ◽  
Alternative Pathway ◽  
Deae Cellulose ◽  
Aminobutyric Acid ◽  
Mammalian Brain ◽  
Aldehyde Dehydrogenases ◽  
Brain Tissues

An enzyme which catalyses dehydrogenation of gamma-aminobutyraldehyde (ABAL) to gamma-aminobutyric acid (GABA) was purified to homogeneity from rat brain tissues by using DEAE-cellulose and affinity chromatography on 5′-AMP-Sepharose, phosphocellulose and Blue Agarose, followed by gel filtration. Such an enzyme was first purified from mammalian brain tissues, and was identified as an isoenzyme of aldehyde dehydrogenase. It has an Mr of 210,000 determined by polyacrylamide-gradient-gel electrophoresis, and appeared to be composed of subunits of Mr 50,000. The close similarity of substrate specificity toward acetaldehyde, propionaldehyde and glycolaldehyde between the enzyme and other aldehyde dehydrogenases previously reported was observed. But substrate specificity of the enzyme toward ABAL was higher than those of aldehyde dehydrogenases from human liver (E1 and E2), and was lower than those of ABAL dehydrogenases from human liver (E3), Escherichia coli and Pseudomonas species. The Mr and relative amino acid composition of the enzyme are also similar to those of E1 and E2. The existence of this enzyme in mammalian brain seems to be related to a glutamate decarboxylase-independent pathway (alternative pathway) for GABA synthesis from putrescine.

Bromoacetophenone as an affinity reagent for human liver aldehyde dehydrogenase

Biochemistry ◽  
1986 ◽  
Vol 25 (18) ◽  
pp. 5182-5189 ◽  
Author(s):  
Alexander D. MacKerell ◽  
Robert S. MacWright ◽  
Regina Pietruszko
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Human Liver ◽  
Affinity Reagent ◽  
Liver Aldehyde Dehydrogenase
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